Yeo Woon-Seok, Lee Soo Jae, Lee Jung Rok, Kim Kwang Pyo
Department of Bioscience and Biotechnology, Konkuk University, Seoul, Korea.
BMB Rep. 2008 Mar 31;41(3):194-203. doi: 10.5483/bmbrep.2008.41.3.194.
Nitrosative modifications regulate cellular signal transduction and pathogenesis of inflammatory responses and neurodegenerative diseases. Protein tyrosine nitration is a biomarker of oxidative stress and also influences protein structure and function. Recent advances in mass spectrometry have made it possible to identify modified proteins and specific modified amino acid residues. For analysis of nitrated peptides with low yields or only a subset of peptides, affinity 'tags' can be bait for 'fishing out' target analytes from complex mixtures. These tagged peptides are then extracted to a solid phase, followed by mass analysis. In this review, we focus on protein tyrosine modifications caused by nitrosative stresses and proteomic methods for selective enrichment and identification of nitrosative protein modifications.
亚硝化修饰调节细胞信号转导以及炎症反应和神经退行性疾病的发病机制。蛋白质酪氨酸硝化是氧化应激的生物标志物,也会影响蛋白质的结构和功能。质谱技术的最新进展使得鉴定修饰蛋白和特定修饰氨基酸残基成为可能。对于低产量的硝化肽或仅部分肽段的分析,亲和“标签”可作为从复杂混合物中“钓出”目标分析物的诱饵。然后将这些带标签的肽段提取到固相上,随后进行质谱分析。在本综述中,我们重点关注亚硝化应激引起的蛋白质酪氨酸修饰以及用于选择性富集和鉴定亚硝化蛋白质修饰的蛋白质组学方法。